Evidence map›Paper›PMID 29573133›Full record

ArticleTraffic (Copenhagen, Denmark)2018

Lipid packing defects and membrane charge control RAB GTPase recruitment.

Guillaume Kulakowski, Hugo Bousquet, Jean-Baptiste Manneville, Patricia Bassereau, Bruno Goud, Lena K Oesterlin

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. ACS chemical biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Lipid rafts, Rab GTPases, and a late endosomal checkpoint for plasma membrane recycling.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. Small but mighty: Atg8s and Rabs in membrane dynamics during autophagy.Biochimica et biophysica acta. Molecular cell research · 2021
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Guillaume KulakowskiInstitut Curie, Paris Sciences et Lettres Research University, Sorbonne Université, CNRS UMR144, Paris, France.
Hugo BousquetInstitut Curie, Paris Sciences et Lettres Research University, Sorbonne Université, CNRS UMR144, Paris, France.
Jean-Baptiste MannevilleInstitut Curie, Paris Sciences et Lettres Research University, Sorbonne Université, CNRS UMR144, Paris, France.
Patricia BassereauLaboratoire Physico Chimie, Institut Curie, Paris Sciences et Lettres Research University, Sorbonne Université, CNRS UMR168, Paris, France.
Bruno GoudInstitut Curie, Paris Sciences et Lettres Research University, Sorbonne Université, CNRS UMR144, Paris, France.
Lena K OesterlinInstitut Curie, Paris Sciences et Lettres Research University, Sorbonne Université, CNRS UMR144, Paris, France.ORCID 0000-0003-3074-2921
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Specific intracellular localization of RAB GTPases has been reported to be dependent on protein factors, but the contribution of the membrane physicochemical properties to this process has been poorly described. Here, we show that three RAB proteins (RAB1/RAB5/RAB6) preferentially bind in vitro to disordered and curved membranes, and that this feature is uniquely dependent on their prenyl group. Our results imply that the addition of a prenyl group confers to RAB proteins, and most probably also to other prenylated proteins, the ability to sense lipid packing defects induced by unsaturated conical-shaped lipids and curvature. Consistently, RAB recruitment increases with the amount of lipid packing defects, further indicating that these defects drive RAB membrane targeting. Membrane binding of RAB35 is also modulated by lipid packing defects but primarily dependent on negatively charged lipids. Our results suggest that a balance between hydrophobic insertion of the prenyl group into lipid packing defects and electrostatic interactions of the RAB C-terminal region with charged membranes tunes the specific intracellular localization of RAB proteins.

Indexed as

HumansMembrane LipidsProtein BindingProtein Prenylationrab GTP-Binding ProteinsStatic ElectricityUnilamellar LiposomesMembrane Lipidsrab GTP-Binding ProteinsUnilamellar Liposomescurvature sensinggeranylgeranyllipid packing defectsmembrane orderprenylation

Identifiers

PMID29573133
PMCPMC6032855
OpenAlexW2791128725

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.